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Disproportionation reactions catalyzed by Leuconostoc and Streptococcus glucansucrases.
Glucansucrases from Leuconostoc mesenteroides NRRL B-512F and Streptococcus mutans 6715 were found to utilize a number of D-gluco-oligosaccharides as D-glucosyl donors and as acceptors, and dextransucrase from S. mutan 6715 was capable of forming alpha-D-(1----3)-linked products.
Fate of Maize DNA During Steeping, Wet-Milling, and Processing
ABSTRACT The fate of DNA during steeping, wet-milling, and subsequent processing of maize was examined using a sensitive polymerase chain reaction (PCR-based) detection system. The system used
Sulfation of benzylic alcohols catalyzed by aryl sulfotransferase IV.
The results of these studies indicated that lipophilicity of the benzylic alcohol was a major factor in determining catalytic efficiency, as represented by the values of kcat/Km, and electronic effects of substituents on the phenyl ring had no effect on the catalysttic efficiency of the enzyme with benzyLic alcohols.
Liquid CO2 as a safe and benign solvent for the ozonolysis of fatty acid methyl esters
We have shown that liquid CO2 dissolves O3 in higher concentrations compared to conventional solvents and is therefore an effective medium for the ozonolysis of unsaturated compounds. The
Assay of purified aryl sulfotransferase suitable for reactions yielding unstable sulfuric acid esters.
Kinetic constants for sulfation of 1-naphthalenemethanol determined by this method compared favorably with those determined using thin-layer chromatographic assays of 35S incorporation, indicating that the method will be suitable for determination of kinetic constants in sulfotransferase-catalyzed reactions where the product sulfuric acid ester may be chemically unstable.
p-nitrophenyl α-d-glucopyranoside, a new substrate for glucansucrases
Abstract p-Nitrophenyl α- d -glucopyranoside has been shown to be a substrate for the glucansucrases of various strains of Leuconostoc mesenteroides and Streptococcus mutans. The products from a
Purification, immunochemical characterization, and immunohistochemical localization of rat hepatic aryl sulfotransferase IV.
A new method for the purification to homogeneity of aryl sulfotransferase IV was developed that provided a greater than 10-fold increase in total yield of enzyme/g of tissue.
Inhibition of Streptococcus mutans 6715 glucosyltransferases by sucrose analogs modified at positions 6 and 6'.
Sucrose derivatives modified at position 6 were tested as inhibitors of the two Streptococcus mutans 6715 glucosyltransferases, and 6-Deoxysucrose was the best inhibitor studied, competitively inhibiting the soluble-D-glucan forming enzyme (GTF-S).
Synthesis of 6-thiosucrose, and an improved route to 6-deoxysucrose.
Inhibition- and acceptor-reaction studies of streptococcus mutans 6715 glucosyltransferases with 3-deoxysucrose, 3-deoxy-3-fluorosucrose, and α-dallopyranosyl β-d-fructofuranoside
Abstract Three new sucrose analogs modified at C-3 have been studied as inhibitors and substrates for the glucosyltransferases (glucansucrases) of Steptococcus mutans 6715. Although none of the